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prolamine/dacsa

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Maize (Zea mays) zeins are some of the most abundant cereal seed storage proteins (SSPs). Their abundance influences kernel hardness but compromises its nutritional quality. Transcription factors regulating the expression of zein and other SSP genes in cereals are endosperm-specific and homologs of

Comprehensive proteomic analysis of developing protein bodies in maize (Zea mays) endosperm provides novel insights into its biogenesis.

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Prolamins, the major cereal seed storage proteins, are sequestered and accumulated in the lumen of the endoplasmic reticulum (ER), and are directly assembled into protein bodies (PBs). The content and composition of prolamins are the key determinants for protein quality and texture-related traits of

In Vitro Synthesis of a Precursor to the Methionine-rich Polypeptide of the Zein Fraction of Corn.

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The messenger ribonucleic acid fraction isolated from a protein bodyenriched fraction of developing corn (Zea mays L.) endosperm stimulated the incorporation of radioactive amino acids into at least five polypeptides when added to a wheat germ extract capable of protein synthesis. Of these, the two

Lysine-rich gamma-zeins are secreted in transgenic Arabidopsis plants.

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We have previously shown that the maize (Zea mays L.) storage prolamine gamma-zein, accumulates in endoplasmic reticulum-derived protein bodies in transgenic plants of Arabidopsis thaliana (L.) ecotype R + P. The retention of gamma-zein in the endoplasmic reticulum was found to be mediated by
The revaluation of the Andean cultivations, quinua (Chenopodium quinua Willd) and lupin (Lupinus albus L.), to be used in nutritional mixtures, with traditional cereals like corn (Zea mays L.) and rice (Oryza sativa L.), originate mixtures without gluten which constitute a good alternative for the
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